Information on EC 1.1.1.336 - UDP-N-acetyl-D-mannosamine dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
1.1.1.336
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RECOMMENDED NAME
GeneOntology No.
UDP-N-acetyl-D-mannosamine dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O = UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Amino sugar and nucleotide sugar metabolism
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UDP-N-acetyl-alpha-D-mannosaminouronate biosynthesis
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metabolism of amino sugars and derivatives
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SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-alpha-D-mannosamine:NAD+ 6-oxidoreductase
Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. The enzyme has no activity with NADP+.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-mannosamine + 2 NAD+ + H2O
UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH + 2 H+
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
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activation at low UDP-N-acetylmannosamine concentrations
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-acetylglucosamine
1.3 mM, 50% inhibition
N-acetylmannosamine
0.07 mM, 50% inhibition
UDP
0.5 mM, 50% inhibition
UDP-glucose
0.6 mM, 50% inhibition
UTP
1 mM, 50% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
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2 mM, maximum activation
N-acetylglucosamine 1-phosphate
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activation at low UDP-N-acetylmannosamine concentrations
tris-(2-carboxyethyl)phosphine hydrochloride
1 mM, about 25% increase in activity
additional information
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the presence of SH compounds is required for activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.21 - 0.57
NAD+
0.11 - 0.38
UDP-N-acetyl-alpha-D-mannosamine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.4
NAD+
Methanococcus maripaludis
Q6LZC3
pH 8.5, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5 - 10
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46100
2 * 46100, calculated
51400
4 * 50000, SDS-PAGE, 4 * 51400, calculated, including His-tag
92000
gel filtration
100000
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gel filtration
200000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 50000, SDS-PAGE, 4 * 51400, calculated, including His-tag
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of the enzyme bound to the product UDP-N-acetyl-alpha-D-mannosaminuronate by X-ray diffraction to resolution of 1.55 A. Crystal structures reveal a tight dimeric polymer chains with product-bound in all the structures. The catalytic residues Cys258 and Lys204 are conserved. The Cys258 acts as catalytic nucleophile and Lys204 as acid/base catalyst. The product directly interacts with residues Arg211, Thr249, Arg244, Gly255, Arg289, Lys319 and Arg398. The SeMet-substituted enzyme is crystallized using microbatch sitting method under reservoir solution condition 10% (w/v) PEG 8000, 8% (v/v) ethylene glycol and 0.1 M HEPES, pH 7.5
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to 1.8 A resolution, space group P21
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18°C, 20 mM Tris-HCl, pH 7.9, 3 M KC1, 2 mM 2-mercaptoethanol, and 10% glycerol, storage without loss of activity for 2 weeks, presence of bovine serum albumin stabilizes
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
gene is not able to complement a defect in the Escherichia coli homologue wecC
Show AA Sequence (877 entries)
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